ArticleJournal of the American Chemical Society2013
Spectral tuning of ultraviolet cone pigments: an interhelical lock mechanism.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 24 citations in OpenAlex.
- Deprotonation of retinal Schiff base and structural dynamics in the early photoreaction of primate blue cone visual pigment.Biophysical journal · 2025Article
- Schiff base deprotonation and structural changes in a mouse UV-sensitive cone visual pigment revealed by FTIR spectroscopy at 77 K.Biophysics and physicobiology · 2025Article
- Glu102Biochemistry · 2024Article
- A short story on how chromophore is hydrolyzed from rhodopsin for recycling.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Review
- Basic and advanced spectrometric methods for complete nanoparticles characterization in bio/eco systems: current status and future prospects.Analytical and bioanalytical chemistry · 2023Review
- Adaptive Landscapes in the Age of Synthetic Biology.Molecular biology and evolution · 2019Review
- Advances in understanding the molecular basis of the first steps in color vision.Progress in retinal and eye research · 2015Review
- The Activation Pathway of Human Rhodopsin in Comparison to Bovine Rhodopsin.The Journal of biological chemistry · 2015Article
- QM/MM model of the mouse olfactory receptor MOR244-3 validated by site-directed mutagenesis experiments.Biophysical journal · 2014Article
- Unusual kinetics of thermal decay of dim-light photoreceptors in vertebrate vision.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Ultraviolet (UV) cone pigments can provide insights into the molecular evolution of vertebrate vision since they are nearer to ancestral pigments than the dim-light rod photoreceptor rhodopsin. While visible-absorbing pigments contain an 11-cis retinyl chromophore with a protonated Schiff-base (PSB11), UV pigments uniquely contain an unprotonated Schiff-base (USB11). Upon F86Y mutation in model UV pigments, both the USB11 and PSB11 forms of the chromophore are found to coexist at physiological pH. The origin of this intriguing equilibrium remains to be understood at the molecular level. Here, we address this phenomenon and the role of the USB11 environment in spectral tuning by combining mutagenesis studies with spectroscopic (UV-vis) and theoretical [DFT-QM/MM (SORCI+Q//B3LYP/6-31G(d): Amber96)] analysis. We compare structural models of the wild-type (WT), F86Y, S90A and S90C mutants of Siberian hamster ultraviolet (SHUV) cone pigment to explore structural rearrangements that stabilize USB11 over PSB11. We find that the PSB11 forms upon F86Y mutation and is stabilized by an "inter-helical lock" (IHL) established by hydrogen-bonding networks between transmembrane (TM) helices TM6, TM2, and TM3 (including water w2c and amino acid residues Y265, F86Y, G117, S118, A114, and E113). The findings implicate the involvement of the IHL in constraining the displacement of TM6, an essential component of the activation of rhodopsin, in the spectral tuning of UV pigments.
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